Evidence map›Paper›PMID 1650581›Full record

ArticleCell regulation1991

Modulation of intercellular adherens-type junctions and tyrosine phosphorylation of their components in RSV-transformed cultured chick lens cells.

T Volberg, B Geiger, R Dror, Y Zick

Open access · greenAbstract read
In one paragraph

Article in Cell regulation, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
6.4field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 161 citations in OpenAlex.

  1. E-Cadherin: A conductor of cellular signaling.Current opinion in cell biology · 2025
    Review
  2. Review
  3. Article
  4. Review
  5. Distinct roles for N-Cadherin linked c-Src and fyn kinases in lens development.Developmental dynamics : an official publication of the American Association of Anatomists · 2013
    Article
  6. The role of MAPK in drug-induced kidney injury.Journal of signal transduction · 2012
    Article
  7. Article
  8. Article
  9. Occludin phosphorylation in regulation of epithelial tight junctions.Annals of the New York Academy of Sciences · 2009
    Article
  10. Article
  11. Review
  12. Cell cycle regulation in the developing lens.Seminars in cell & developmental biology · 2006
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

T VolbergDepartment of Chemical Immunology, Weizmann Institute of Science Rehovot, Israel.
B Geiger
R Dror
Y Zick
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transformation of cultured chick lens epithelial cells with a temperature-sensitive mutant of Rous sarcoma virus (tsRSV) leads to radical changes in cell shape and interactions. When cultured at the restrictive temperature (42 degrees C), the transformed cells largely retained epithelial morphology and intercellular adherens junctions (AJ), whereas on switch to the permissive temperature (37 degrees C) they rapidly became fibroblastoid, their AJ deteriorated, and cell adhesion molecules (A-CAM) (N-cadherin) largely disappeared from intercellular contact sites. The microfilament system that was primarily associated with these junctions was markedly rearranged on shift to 37 degrees C and remained associated mainly with cell-substrate focal contacts. These apparent changes in intercellular AJ were not accompanied by significant alterations in the cellular content of several junction-associated molecules, including A-CAM, vinculin, and talin. Immunolabeling with phosphotyrosine-specific antibodies indicated that both cell-substrate and intercellular AJ were the major cellular targets for the pp60v-src tyrosine-specific protein kinase. It was further shown that intercellular AJ components serve as substrates to tyrosine kinases also in nontransformed lens cells, because the addition of a combination of vanadate and H2O2--which are potent inhibitors of protein tyrosine phosphatases--leads to a remarkable accumulation of immunoreactive phosphotyrosine-containing proteins in these junctions. This finding suggests that intercellular junctions are major sites of action of protein tyrosine kinases and that protein tyrosine phosphatases play a major role in the regulation of phosphotyrosine levels in AJ of both normal and RSV-transformed cells.

Indexed as

Cell Transformation, ViralAnimalsAvian Sarcoma VirusesCell AdhesionCells, CulturedIntercellular JunctionsLens, CrystallineMicroscopy, ElectronMutationPhosphoprotein PhosphatasesPhosphorylationProtein-Tyrosine KinasesProtein Tyrosine PhosphatasesTemperatureTyrosinePhosphoprotein PhosphatasesProtein-Tyrosine KinasesProtein Tyrosine PhosphatasesTyrosine

Identifiers

PMID1650581
PMCPMC361726
OpenAlexW2022504141

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.